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Database: UniProt
Entry: W1TL89_9ACTO
LinkDB: W1TL89_9ACTO
Original site: W1TL89_9ACTO 
ID   W1TL89_9ACTO            Unreviewed;       470 AA.
AC   W1TL89;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=Q618_VCMC00002G0063 {ECO:0000313|EMBL:ETI82241.1};
OS   Varibaculum cambriense DORA_20.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Varibaculum.
OX   NCBI_TaxID=1403948 {ECO:0000313|EMBL:ETI82241.1, ECO:0000313|Proteomes:UP000018843};
RN   [1] {ECO:0000313|EMBL:ETI82241.1, ECO:0000313|Proteomes:UP000018843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_20 {ECO:0000313|Proteomes:UP000018843};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant
RT   gut community with otherwise low bacterial novelty that shifts toward
RT   anaerobic metabolism during the third week of life.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETI82241.1}.
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DR   EMBL; AZMI01000002; ETI82241.1; -; Genomic_DNA.
DR   PATRIC; fig|1403948.3.peg.1523; -.
DR   Proteomes; UP000018843; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018843}.
FT   DOMAIN      160    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      372    441       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   470 AA;  52835 MW;  3F8C64F81FF16EC4 CRC64;
     MSSSLQSVWQ DAIRQLKQNP QVGQADLAFV RMSKPLTTYE NTIIIATPNN YSKSIIETRL
     APFLRQSLSA ATSRDVILAV SVDPSLDTGQ TVNPSEHQTV APLPQKSEST TTKTTTASRE
     KKPFESRLNS KYTFESFVIG ASNRFAHAAA IAVAEAPAKA YNPLFVYGGS GLGKTHLLHA
     IGNYALNLYP HIKVRYVNSE EFTNDFINSV SEGSAHEFQR RYRNIDILMI DDIQFLQGKE
     QTIEEFFHTF NSLHNDNKQV VITSDVPPKK LEGFEERLRS RFEWGLLTDV QPPDLETRIA
     ILRNKIRQEK VEAPSEVLAY IASRFTINIR ELEGALLRVT AFASLTKQPL TLQLAEMVLK
     DIVSDPNDQE ITPALIKAQT AGYFETTVND LCSPSRSRSL TEARQIAMYL CRELTELSLP
     QIGKEFGGRD HTTVMHANKK ITQLMKSKPQ IFDHVNELTN QIRQAARHAK
//
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